Mycobacteria, including Mycobacterium tuberculosis, have developed strains that resist contemporary multi-drug treatment regimes. With nearly two million yearly deaths caused by infections of M. tuberculosis and with more than 200,000 people debilitated by infections of M. leprae there is concerted need to understand the mechanisms of Mycobacterial resilience. Part of the persistence and lethality of these diseases is due to the impermeable mycobacteria cell wall. Mycobacteria's unique ˜8 nm thick outer cellular casing has far lower permeability to hydrophilic agents than Escherichia coli's cell wall and is a key factor in the drug and environmental resistance of mycobacteria. 
Although containing other constituents, the mycobacterial outer membrane contains 30%-40% mycolic acids. Mycolic acids contain a carboxylic acid headgroup with two hydrophobic tails of unequal length. See FIG. 1 for exemplary mycolic acids. In vivo, mycolic acids are covalently linked by the carboxylate group to peptidoglycans or trehalose sugars. The significant impermeability of the mycobacterial membranes results in the need for pathways for hydrophilic solutes. This pathway is mediated by protein pores.
In vivo studies of pore proteins in the mycobacterial cell-wall of M. smegmatis, a close relative of M. tuberculosis, led to the discovery of the outer membrane pore M. smegmatis porin A (MspA). In M. smegmatis, MspA is the most abundant protein and forms the primary pathway for hydrophilic nutrients to traverse the outer membrane. OmpATb, another protein pore, and ion transporters have been isolated in mycobacterium species but their behavior in their natural environment remains unexplored.
To investigate various properties of pores, such pores are often embedded in membranes. There is a need to develop suitable membranes for these and other experiments involving mycolic acid membranes.